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Emulsion products with natural antimicrobials are becoming increasingly popular for topical application. Mandelic Acid is interesting in cosmetics due to its potent exfoliating properties, which have driven advancements in skincare technologies. Essential oils have various properties, of which the most useful in cosmetics are those that do not cause irritation, smell pleasant, and have other beneficial properties such as antimicrobial effects. Emulsions with Mandelic Acid and essential oils from Satureja montana, Lemongrass, and Litsea cubeba were formulated and microbiologically tested for their preservative effectiveness. The effect of the treatments on skin condition was monitored by non-invasive diagnostic methods, such as hydration, transepidermal water loss, and pH value. Sensory analysis revealed that the matrix containing Mandelic Acid alone or combined with Litsea Cubeba Oil was the best-performing formulation, consistent with the compliant results of antimicrobial efficacy. The topical form of this cosmetic product has demonstrated excellent preservative activity and desirable biophysical efficacy on the skin.

The application of biopolymer-based materials is increasing due to better sustainability and environmental protection properties. Gelatin fibers have a specific surface and high porosity, which is why their use in medicine and the food industry is being researched. This article explores the potential of centrifugal spinning to produce gelatin fibers. Gelatin for fiber preparation was obtained from a non-traditional source of collagen (chicken by-products) using a unique enzymatic process. The fiber quality was compared with those prepared from gelatins produced from traditional collagen tissues (porcine, bovine). The results showed that fibers cross-linked with glutaraldehyde vapor preserved their structure even in contact with water. Using a cross-linker controlled swelling ability and solubility while maintaining the fiber structure. On the contrary, uncross-linked gelatin fibers were water soluble due to a high surface-to-volume ratio, facilitating water penetration and dissolution. Scanning electron microscopy (SEM) provided a clearer picture of the morphology of gelatin fibers obtained by centrifugal spinning. Differences in the amount of bonding depending on the raw material used and the presence of a cross-linker were analyzed using Fourier transform infrared spectroscopy (FTIR). The overall results showed that chicken gelatin is a suitable alternative to gelatins from traditional sources and can be used for preparing food and pharmaceutical packaging and coatings, fibers, or bioprinting of 3D matrices.

In most cases, the unused by-products of venison, including deer tallow, are disposed of in rendering plants. Deer tallow contains essential fatty acids and can be used to prepare products for everyday food and advanced applications. This work aimed to process deer tallow into hydrolyzed products using microbial lipases. A Taguchi design with three process factors at three levels was used to optimize the processing: amount of water (8, 16, 24%), amount of enzyme (2, 4, 6%), and reaction time (2, 4, 6 h). The conversion of the tallow to hydrolyzed products was expressed by the degree of hydrolysis. The oxidative stability of the prepared products was determined by the peroxide value and the free fatty acids by the acid value; further, color change, textural properties (hardness, spreadability, stickiness, and adhesiveness), and changes at the molecular level were observed by Fourier transform infrared spectroscopy (FTIR). The degree of hydrolysis was 11.8–49.6%; the peroxide value ranged from 12.3 to 29.5 µval/g, and the color change of the samples expressed by the change in the total color difference (∆E*) was 1.9–13.5. The conditions of enzymatic hydrolysis strongly influenced the textural properties: hardness 25–50 N, spreadability 20–40 N/s, and stickiness < 0.06 N. FTIR showed that there are changes at the molecular level manifested by a decrease in ester bonds. Enzymatically hydrolyzed deer tallow is suitable for preparing cosmetics and pharmaceutical matrices.

Chicken collagen is a promising raw material source for the production gelatins and hydrolysates. These can be prepared biotechnologically using proteolytic enzymes. By choosing the appropriate process conditions, such changes can be achieved at the molecular level of collagen, making it possible to prepare gelatins with targeted properties for advanced cosmetic, pharmaceutical, medical, or food applications. The present research aims to investigate model samples of chicken gelatins, focusing on: (i) antioxidant activity using 2,2-diphenyl-1-picrylhydrazyl (DPPH) and 2,2-azinobis-3-etylbenzotiazolin-6-sulfonic acid (ABTS); (ii) the distribution of molecular weights via gel permeation chromatography with refractometric detection (GPC-RID); (iii) functional groups and the configuration of polypeptide chains related to molecular-level properties using Fourier transform infrared spectroscopy (FTIR); (iv) the microbiological populations on sabouraud dextrose agar (SDA), plate count agar (PCA), tryptic soy agar (TSA), and violet red bile lactose (VRBL) using the matrix-assisted laser desorption ionization (MALDI) method. Antioxidant activity towards ABTS radicals was more than 80%; activity towards DPPH radicals was more than 69%. The molecular weights of all gelatin samples showed typical α-, β-, and γ-chains. FTIR analysis confirmed that chicken gelatins all contain typical vibrational regions for collagen cleavage products, Amides A and B, and Amides I, II, and III, at characteristic wavenumbers. A microbiological analysis of the prepared samples showed no undesirable bacteria that would limit advanced applications of the prepared products. Chicken gelatins represent a promising alternative to products made from standard collagen tissues of terrestrial animals.

Sous-vide is a process comprising vacuum-sealing food, heating it to the desired temperature, and circulating it in a water bath in a sous vide machine. This cooking technique is increasingly common in homes and catering establishments due to its simplicity and affordability. However, manufacturers and chef’s recommendations for low-temperature and long-term sous-vide cooking in media raise food safety concerns, particularly when preparing beef tenderloin. In this study, Salmonella enterica was found to be inactivated by heat and sage essential oil (EO) in beef samples from musculus psoas major that had been sous vide processed. To determine whether heat treatment was likely to increase the sous vide efficiency, S. enterica and sage EO were mixed. After being vacuum-packed and injected with S. enterica, the samples were cooked at 50–65 °C through the sous vide technique for the prescribed time. On days 1, 3, and 6, the amounts of S. enterica, total bacteria, and coliform bacteria were measured in the control and treated groups of beef processed sous vide. Mass spectrometry was used to identify bacterial isolates on different days. On each day that was measured, a higher number of all the microbiota was found in the samples exposed to 50 °C for 5 min. The most frequently isolated microorganisms from both groups of samples were Pseudomonas fragi (17%), Pseudomonas cedrina (8%), and Proteus vulgaris (8%); in the treated group, also S. enterica (21%), Pseudomonas fragi (13%), and Pseudomonas veronii (6%). After the heat treatment of samples at 65 °C for 20 min, the total count of bacteria and coliform bacteria was zero. It has been shown that adding sage essential oil (EO) in combination with sous vide processing technique leads to the stabilization and safety of beef tenderloin.

Comedogenic skin care receives little attention compared to the care or treatment of more serious acne manifestations. Traditional therapies may have limited success with potential side effects. Cosmetic care supported by the effect of a biostimulating laser may offer a desirable alternative. The aim of the study was to evaluate the biological effectiveness of combined cosmetic treatment with lasotherapy on comedogenic skin type using noninvasive bioengineering methods. Twelve volunteers with comedogenic skin type underwent a 28-week application of Lasocare Basic 645® cosmetic gel containing Lactoperoxidase and Lactoferrin in combination with laser therapy (Lasocare® method). The effect of treatment on skin condition was monitored using noninvasive diagnostic methods. The parameters were the amount of sebum, the pore count, the ultraviolet-induced red fluorescence assessment of comedonic lesions (percentage of the area and quantification of orange-red spots), hydration, transepidermal water loss, and pH. A statistically significant decrease in sebum production was observed on the skin of the treated volunteers, as well as a decrease in porphyrins, indicating the presence of Cutibacterium acnes populating comedones and causing enlarged pores. The balance of epidermal water in the skin was regulated adjusting the acidity of the skin coat in individual zones, which decreased the presence of Cutibacterium acnes. Cosmetic treatment in combination with the Lasocare® method successfully improved the condition of comedogenic skin. In addition to transient erythema, there were no other adverse effects. The chosen procedure appears to be a suitable and safe alternative to traditional treatment procedures known from dermatological practice.

Chicken stomachs are by-products obtained from the poultry processing in slaughterhouses. Their amount has been gradually increasing as a consequence of a continually rising poultry consumption. Since these animal tissues are still rich in proteins, mainly collagen, fat, and minerals, it is essential and beneficial to investigate the appropriate management and further processing. Collagen could be extracted from chicken stomachs and used as a raw material in the food, cosmetic, medical, and also pharmaceutical industry. This paper is to investigate possibilities of such extraction of collagen products, gelatines, or alternatively hydrolysates, from chicken stomachs after prior biotechnological treatment with the proteolytic enzyme Protamex. In this experiment, non-collagenous proteins were removed from stomachs using 0.03 M NaOH and 0.2 M NaCl. Subsequently, the tissue was defatted applying acetone and the enzyme Lipolase. Purified and dried collagen was then treated with the proteolytic enzyme Protamex. In the last step, gelatine was extracted from the tissue in hot water. The influence of selected processing parameters on the extraction efficiency and final product quality was monitored. The extraction conditions included the amount of the added enzyme (0.1 – 0.4%) and the extraction temperature of between 60 and 65 °C. The total gelatine yield ranged from 43.80 to 96.45% and the gel strength varied from 2 ±0 to 429 ±8 Bloom. The enzymatic treatment of the raw material is an economical and ecological alternative to traditional acid or alkaline treatments. Extracted gelatine with the gel strength of 100 – 300 Bloom would be suitable for the applications in the food industry in the production of confectionery, marshmallow, aspic or dairy products.

Gelatine is, due to its functional properties, currently widely used not only in the food industry (in the production of confectionery, dairy products, canned food) but also in pharmacy (soft and hard capsules) and cosmetics (creams, lotions) where it applies its ability to form thermoreversible gel stronger than most other gelling agents. What is more, it provides further excellent properties including emulsifying, foaming, stabilizing, film-forming, water and fat binding, texturizing, thickening, and adhesive attributes which makes it a very important hydrocolloid. Gelatine is obtained from the raw material of animal tissues containing collagen, usually mammalian skin or bones. For religious reasons in some countries, pork or bovine gelatine must be replaced by an alternative form, such as poultry or fish gelatine. The quality of gelatine is assessed mostly by the strength of gelatine gel which strongly depends on ambient temperature or humidity. Extraction conditions may also significantly affect the quality of gelatine. This study examined possible changes in the strength of gelatine gels prepared from laboratory-produced chicken feet gelatine and compared them with commercially available pork and beef gelatines at temperatures of 23, 29, and 35 °C at 60 and 80% humidity. While at 23 °C thermal stability of prepared chicken gelatine was monitored higher than in commercial gelatines, experiments at 29 and 35 °C provided equivalent results for chicken and commercial gelatines. Therefore, prepared chicken gelatine offers a significant potential to become an alternative to traditional gelatines. The information about gelatine gels thermal stability is of great importance for applications not only in the food; but also in the pharmaceutical industry.

During the production of mechanically deboned chicken meat (MDCM), a by-product is created that has no adequate use and is mostly disposed of in rendering plants. Due to the high content of collagen, it is a suitable raw material for the production of gelatin and hydrolysates. The purpose of the paper was to process the MDCM by-product into gelatin by 3-step extraction. An innovative method was used to prepare the starting raw material for gelatin extraction, demineralization in HCl, and conditioning with a proteolytic enzyme. A Taguchi design with two process factors (extraction temperature and extraction time) was used at three levels (42, 46, and 50 °C; 20, 40, and 60 min) to optimize the processing of the MDCM by-product into gelatins. The gel-forming and surface properties of the prepared gelatins were analyzed in detail. Depending on the processing conditions, gelatins are prepared with a gel strength of up to 390 Bloom, a viscosity of 0.9–6.8 mPa·s, a melting point of 29.9–38.4 °C, a gelling point of 14.9–17.6 °C, excellent water- and fat-holding capacity, and good foaming and emulsifying capacity and stability. The advantage of MDCM by-product processing technology is a very high degree of conversion (up to 77%) of the starting collagen raw material to gelatins and the preparation of 3 qualitatively different gelatin fractions suitable for a wide range of food, pharmaceutical, and cosmetic applications. Gelatins prepared from MDCM by-product can expand the offer of gelatins from other than beef and pork tissues.

Antimicrobial hand gels have become extremely popular in recent years due to the COVID-19 pandemic. Frequent use of hand sanitising gel can lead to dryness and irritation of the skin. This work focuses on the preparation of antimicrobial acrylic acid (Carbomer)-based gels enhanced by non-traditional compounds—mandelic acid and essential oils—as a substitute for irritating ethanol. Physicochemical properties (pH and viscosity), stability and sensory attributes of the prepared gels were investigated. Antimicrobial activity against representative Gram-positive and Gram-negative bacteria and yeasts was determined. The prepared gels with mandelic acid and essential oil (cinnamon, clove, lemon, and thyme) proved to have antimicrobial activity and even better organoleptic properties than commercial ethanol-based antimicrobial gel. Further, results confirmed that the addition of mandelic acid had a desirable effect on gel properties (antimicrobial, consistency, stability). It has been shown that the essential oil/mandelic acid combination can be a dermatologically beneficial hand sanitiser compared to commercial products. Thus, the produced gels can be used as a natural alternative to alcohol-based daily hand hygiene sanitisers.

With the increasing consumption of poultry meat around the world, the use of chicken stomachs as a source of collagen is being offered. The objective of this study was to extract gelatin from the stomachs of broiler chickens and to estimate their gel strength, ash content, viscosity, gelling point, melting point, clarity and digestibility. An innovative biotechnological method based on the conditioning of collagen with a microbial endoproteinase (Protamex®) and hot-water extraction was used to control the chemical and thermal denaturation process of collagen to prepare gelatin. The experiments were planned using a Taguchi design, 2 factors at 3 levels; factor A for the amount of proteolytic enzyme (0.10, 0.15 and 0.20%) and factor B for the extraction temperature (55.0, 62.5 and 70.0 °C). Data were statistically processed and analyzed at a significance level of 95%. The gelatin yield averaged 65 ± 8%; the gel strength ranged from 25 ± 1 to 439 ± 6 Bloom, the viscosity from 1.0 ± 0.4 to 3.40 ± 0.03 mPa·s, gelling point from 14.0 ± 2.0 to 22.0 ± 2.0 °C, melting point from 28.0 ± 1.0 to 37.0 ± 1.0 °C. The digestibility of gelatin was 100.0% in all samples; the ash content was very low (0.44 ± 0.02–0.81 ± 0.02%). The optimal conditions for the enzymatic treatment of collagen from chicken stomachs were achieved at a higher temperature (70.0 °C) and a lower amount of enzyme (0.10–0.15%). Conditioning chicken collagen with a microbial endoproteinase is an economically and environmentally friendly processing method, an alternative to the usual acid- or alkaline-based treatment that is used industrially. The extracted products can be used for food and pharmaceutical applications.

Byproducts obtained from fish processing account for up to 70% of their live weight and represent a large amount of unused raw materials rich in proteins, fats, minerals, and vitamins. Recently, the management of the use of predominantly cold-water fish byproducts has become a priority for many processing companies. This paper describes the biotechnological processing of byproducts of warm-water Cyprinus carpio skeletons into gelatins. A Taguchi experimental design with two process factors (HCl concentration during demineralization of the starting material and the amount of enzyme during enzyme conditioning of the collagen) examined at three levels (0.5, 1.0 and 2.0 wt%; 0.0, 0.1 and 0.2 wt% respectively) was used to optimize the processing of fish tissue into gelatin. Depending on the preparation conditions, four gelatin fractions were prepared by multi-stage extraction from the starting material with a total yield of 18.7–55.7%. Extensive characterization of the gel-forming and surface properties of the prepared gelatins was performed. Gelatins belong to the group of zero–low-medium Bloom value (0–170 Bloom) and low–medium viscosity (1.1–4.9 mPa·s) gelatins and are suitable for some food, pharmaceutical, and cosmetic applications. During processing, the pigment can be isolated; the remaining solid product can then be used in agriculture, and H3PO4Ca can be precipitated from the liquid byproduct after demineralization. The carp byproduct processing technology is environmentally friendly and meets the requirements of zero-waste technology.

Poultry meat-processing industry produces considerably large amounts of by-products (such as chicken skins, heads, feathers, viscera, bones and legs) containing significant volumes of proteins, particularly collagen. One of the possibilities of advantageous utilization of these under-used by-products can be their application as a raw material rich in collagen for preparation of gelatine, a partial hydrolysate of collagen. In the present study, chicken skins obtained as a by-product from the chicken-breast processing were purified from non-collagen proteins, pigments and fats. Collagen was treated with proteolytic enzymes and the gelatine extraction was performed in distilled water at temperatures of 40, 50, 60, 70 and 80 °C during the constant extraction time of 60 min. The influence of the technological conditions on gelatine functional properties including viscosity, clarity, water holding and fat binding capacity, emulsifying and foaming properties was explored. Certain functional properties of prepared gelatines were significantly affected by the extraction temperature, while on some other properties the extraction temperature had no significant effect. Viscosity of prepared chicken skin gelatines was in the range from 3 to 5.7 mPa.s, clarity from 1.5 to 2%, water holding capacity from 3.8 to 5.6 mL.g-1, fat binding capacity from 0.9 to 1.3 mL.g-1, emulsion capacity from 35 to 50%, emulsion stability from 73 to 88%, foaming capacity from 18 to 61% and finally foaming stability was from 4 to 39%. Chicken skin gelatines were compared with commercial food grade pork and beef gelatines. Prepared chicken skin gelatines showed better viscosity, fat binding capacity and foaming stability than mammalian gelatines, while water holding capacity, emulsifying stability and foaming capacity were not as good as in beef and pork gelatines. Emulsifying capacity was comparable with commercial gelatines. Therefore, chicken skin gelatine has the potential as an alternative to traditional gelatines from mammalian sources, such as pork or beef bones and skins.

Chicken stomachs can be processed into collagen hydrolysate usable in cosmetic products. The aim of the study was to verify the effects of a carbopol gel formulation enriched with 1.0% (w/w) chicken hydrolysate on the properties of the skin in the periorbital area after regular application twice a day for eight weeks in volunteers ageed 50 ± 9 years. Skin hydration, transepidermal water loss (TEWL), skin elasticity and skin relief were evaluated. Overall, skin hydration increased by 11.82% and 9.45%, TEWL decreased by 25.70% and 17.80% (always reported for the right and left area). Generally, there was an increase in skin elasticity, a decrease in skin roughness, as the resonance times decreased by 85%. The average reduction of wrinkles was 35.40% on the right and 41.20% on the left. For all results, it can be seen that the longer the cosmetic gel formulation is applied, the better the results. Due to the positive effect on the quality and functionality of the skin, it is possible to apply the cosmetic gel formulation in the periorbital area. The advantage of the product with chicken collagen hydrolysate is also the biocompatibility with the skin and the biodegradability of the formulation.

In recent decades, food waste management has become a key priority of industrial and food companies, state authorities and consumers as well. The paper describes the biotechnological processing of mechanically deboned chicken meat (MDCM) by-product, rich in collagen, into gelatins. A factorial design at two levels was used to study three selected process conditions (enzyme conditioning time, gelatin extraction temperature and gelatin extraction time). The efficiency of the technological process of valorization of MDCM by-product into gelatins was evaluated by % conversion of the by-product into gelatins and some qualitative parameters of gelatins (gel strength, viscosity and ash content). Under optimal processing conditions (48–72 h of enzyme conditioning time, 73–78 °C gelatin extraction temperature and 100–150 min gelatin extraction time), MDCM by-product can be processed with 30–32% efficiency into gelatins with a gel strength of 140 Bloom, a viscosity of 2.5 mPa.s and an ash content of 5.0% (which can be reduced by deionization using ion-exchange resins). MDCM is a promising food by-product for valorization into gelatins, which have potential applications in food-, pharmaceutical- and cosmetic fields. The presented technology contributes not only to food sustainability but also to the model of a circular economy.

Honey, honey extracts, and bee products belong to traditionally used bioactive molecules in many areas. The aim of the study was primarily to evaluate the effect of cosmetic matrices containing honey and bee products on the skin. The study is complemented by a questionnaire survey on the knowledge and awareness of the effects and potential uses of bee products. The effect of bee molecules at various concentrations was observed by applying 12 formulations to the skin of the volar side of the forearm by non-invasive bioengineering methods on a set of 24 volunteers for 48 h. Very good moisturizing properties have been found in matrices with the glycerin extract of honey. Matrices containing forest honey had better moisturizing effects than those containing flower honey. Barrier properties were enhanced by gradual absorption, especially in formulations with both glycerin and aqueous honey extract. The observed organoleptic properties of the matrices assessed by sensory analysis through 12 evaluators did not show statistically significant differences except for color and spreadability. There are differences in the ability to hydrate the skin, reduce the loss of epidermal water, and affect the pH of the skin surface, including the organoleptic properties between honey and bee product matrices according to their type and concentration.

Every year, the poultry industry produces a large number of by-products such as chicken heads containing a considerable proportion of proteins, particularly collagen. To prepare gelatin is one of the possibilities to advantageously utilize these by-products as raw materials. The aim of the paper was to process chicken heads into gelatins. An innovative method for conditioning starting raw material was using the proteolytic enzyme. Three technological factors influencing the yield and properties of extracted gelatins were monitored including the amount of enzyme used in the conditioning of the raw material (0.4% and 1.6%), the time of the conditioning (18 and 48 h), and the first gelatin extraction time (1 and 4 h). The gelatin yield was between 20% and 36%. The gelatin gel strength ranged from 113 to 355 Bloom. The viscosity of the gelatin solution was determined between 1.4 and 9.5 mPa.s. The content of inorganic solids varied from 2.3% to 3.9% and the melting point of the gelatin gel was recorded between 34.5 and 42.2 °C. This study has shown that gelatin obtained from chicken heads has a promising potential with diverse possible applications in the food industry, pharmacy, and cosmetics.

The aim of the paper is to test stability and biophysical properties of hydrophilic and lipophilic emulsions with selected vegetable seed oils: Limnanthes alba, Prunus amygdalus dulcis, Cannabis sativa, Rosa rubiginosa and Hellianthus annuus. Biophysical properties of emulsions are investigated in vivo using non-invasive instrumental methods (corneometry, tewametry and pH) in a group of 12 healthy women volunteers. Their stability profiles (colour, phase separation and centrifugation) under various temperatures (9, 25, 37 and 57 °C) and storage time (24 hours, 2, 7, 14, 21 and 28 days) were monitored. The moisturising activities of the emulsions supplemented with various oils were comparable. The lipophilic emulsions showed a better ability to improve the condition of the skin barrier due to formation of a surface lipid film. The tested formulations regulated the pH of the skin towards neutral values. Lipophilic emulsions showed earlier phase separation and changes in colour. The greatest resistance to thermal stress during storage was observed for the emulsion bases. Emulsions containing oils, except for those with rosehip and hempseed oils, were stable up to the temperature of 37 °C. The studied emulsion systems are excellent vehicles of vegetable oils and exhibit relatively good stability, benefiting the natural properties of skin.

In the European Union (EU), about five tons of poultry by-product tissues are produced every year. Due to their high collagen content, they represent a significant raw material source for gelatine production. The aim of the paper was the biotechnological preparation of gelatine from chicken feet. The influence of selected process factors on the gelatine yield, gel strength, viscosity, and ash of gelatine was observed; a two-level factor design of experiments with three variable process factors (enzyme addition, enzyme treatment time, and gelatine extraction time) was applied. After grinding and separating soluble proteins and fat, the purified raw material was treated in water at pH 7.5 with the addition of endoprotease at 23 °C and after thorough washing with water at 80 °C, gelatine was extracted. By the suitable choice of process conditions, gelatine with high gel strength (220−320 bloom), low ash content (

Although keratin hydrolysates (KH) are added to skin care agents, detailed studies on the moisturising effects of KH are lacking. The aim of this study is to test whether adding KH into an ointment base (OB) heighten hydration of the skin and diminish transepidermal loss of water (TEWL). Formulations containing 2%, 4%, and 6% of KH (based on OB weight) were prepared. Hydration, TEWL and skin pH were measured; intervals of measurements were as follows: 1, 2, 3, 4, 24 and 48 h. Testing was carried out on 10 men. In terms of hydration, supplementing the OB with 2% KH is optimal, as an 11⁻19% increase occurs in hydration of stratum corneum (SC). All the formulations with added KH as tested caused TEWL to decline after application. Keratin hydrolysate makes for an excellent occlusive; adding it to OB results in a 30⁻50% reduction in TEWL after application. KH functions as a humectant as well, as it helps to bind water from the lower layers of the epidermis to the SC. Formulations with additions of 2⁻6% of KH were stable in structure and did not cause phase separation even after 6 months storage.

Freezing is one of the oldest and most-often-used traditional methods to prolong the shelf life of meat. However, the negative phenomenon of this process is the weight loss of water that occurs after the meat is thawed. Together with the water that escapes from the meat during thawing, there are large weight losses in this valuable raw material. Another negative aspect is that mineral and extractive substances, vitamins, etc. also leave the meat, resulting in irreversible nutritional losses of nutrients in the meat, which are subsequently missing for use by the consumer of the meat. The main goal of this work is to reduce these losses by using gelatin coatings. Gelatin was prepared from chicken paws according to a patented biotechnological procedure, which uses the very gentle principle of obtaining gelatin with the usage of enzymes. This unique method is friendly to the environment and innocuous for the product itself. At the same time, it ensures that the required principles achieve a circular economy with the use of the so far very-little-used slaughter byproducts, which in most parts of the world end up in uneconomic disposal by burning or landfilling without using this unique potential source of nutrients. Gelatin coatings on the surface of the beef steak were created by immersing the meat in a solution based on gelatin of different composition. A coating containing 3%, 5% or 8% gelatin with 10% or 20% glycerol (by weight of gelatin) and 1% glutaraldehyde crosslinker (by weight of gelatin) has proved to be effective. The amount of glutaraldehyde added to the coating is guaranteed not to exceed the permitted EU/U.S. legislative limits. In addition to weight loss, meat pH, color and texture were also measured. Freezing was done in two ways; some samples were frozen at a normal freezing temperature of −18 °C and the other part of the experiment at deep (shock) freezing at −80 °C. Defrosting took place in two ways, in the refrigerator and in the microwave oven, in order to use the common defrosting methods used in gastronomy. A positive effect of this coating on weight loss was observed for each group of samples. The most pronounced effect of coating was found for the least gentle method of freezing (−18 °C) and thawing (microwave), with the average weight loss of the coated samples differing by more than 2% from that of the uncoated sample. No negative effect of the coating was observed for other meat properties tested, such as pH, Warner-Bratzler Shear Force (WBSF) or color. Gelatin-based coating has a positive effect on reducing the weight loss of meat after thawing. Chicken gelatin prepared by a biotechnological process has a new application in improving the quality of meat due to the retention of water and nutrients in frozen and subsequently thawed beef, which can contribute to the better quality of the subsequently gastronomically prepared dish, while maintaining the weight and nutritional quality. This also results in economic savings in the preparation of highly-valued parts of beef.